ID   UDB17_HUMAN             Reviewed;         530 AA.
AC   O75795;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   13-FEB-2019, entry version 145.
DE   RecName: Full=UDP-glucuronosyltransferase 2B17;
DE            Short=UDPGT 2B17;
DE            EC=2.4.1.17;
DE   AltName: Full=C19-steroid-specific UDP-glucuronosyltransferase;
DE            Short=C19-steroid-specific UDPGT;
DE   Flags: Precursor;
GN   Name=UGT2B17;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Prostate;
RX   PubMed=8798464; DOI=10.1074/jbc.271.37.22855;
RA   Beaulieu M., Levesque E., Hum D.W., Belanger A.;
RT   "Isolation and characterization of a novel cDNA encoding a human UDP-
RT   glucuronosyltransferase active on C19 steroids.";
RL   J. Biol. Chem. 271:22855-22862(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9364925; DOI=10.1089/dna.1997.16.1143;
RA   Beaulieu M., Levesque E., Tchernof A., Beatty B.G., Belanger A.,
RA   Hum D.W.;
RT   "Chromosomal localization, structure, and regulation of the UGT2B17
RT   gene, encoding a C19 steroid metabolizing enzyme.";
RL   DNA Cell Biol. 16:1143-1154(1997).
RN   [3]
RP   INVOLVEMENT IN BONE MINERAL DENSITY VARIANCE.
RX   PubMed=18992858; DOI=10.1016/j.ajhg.2008.10.006;
RA   Yang T.-L., Chen X.-D., Guo Y., Lei S.-F., Wang J.-T., Zhou Q.,
RA   Pan F., Chen Y., Zhang Z.-X., Dong S.-S., Xu X.-H., Yan H., Liu X.,
RA   Qiu C., Zhu X.-Z., Chen T., Li M., Zhang H., Zhang L., Drees B.M.,
RA   Hamilton J.J., Papasian C.J., Recker R.R., Song X.-P., Cheng J.,
RA   Deng H.-W.;
RT   "Genome-wide copy-number-variation study identified a susceptibility
RT   gene, UGT2B17, for osteoporosis.";
RL   Am. J. Hum. Genet. 83:663-674(2008).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: UDPGT is of major importance in the conjugation and
CC       subsequent elimination of potentially toxic xenobiotics and
CC       endogenous compounds. The major substrates of this isozyme are
CC       eugenol > 4-methylumbelliferone > dihydrotestosterone (DHT) >
CC       androstane-3-alpha,17-beta-diol (3-alpha-diol) > testosterone >
CC       androsterone (ADT).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor
CC         beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17;
CC   -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000305}; Single-
CC       pass membrane protein {ECO:0000305}. Endoplasmic reticulum
CC       membrane {ECO:0000305}; Single-pass membrane protein
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in various tissues including the
CC       liver, kidney, testis, uterus, placenta, mammary gland, adrenal
CC       gland, skin and prostate.
CC   -!- POLYMORPHISM: Copy-number variation of UGT2B17 defines the bone
CC       mineral density quantitative trait locus 12 (BMND12) [MIM:612560].
CC       Variance in bone mineral density is a susceptibility factor for
CC       osteoporotic fractures. {ECO:0000269|PubMed:18992858}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; U59209; AAC25491.1; -; mRNA.
DR   CCDS; CCDS3523.1; -.
DR   RefSeq; NP_001068.1; NM_001077.3.
DR   UniGene; Hs.575083; -.
DR   ProteinModelPortal; O75795; -.
DR   SMR; O75795; -.
DR   STRING; 9606.ENSP00000320401; -.
DR   BindingDB; O75795; -.
DR   ChEMBL; CHEMBL4978; -.
DR   DrugBank; DB00678; Losartan.
DR   SwissLipids; SLP:000001696; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   iPTMnet; O75795; -.
DR   PhosphoSitePlus; O75795; -.
DR   BioMuta; UGT2B17; -.
DR   jPOST; O75795; -.
DR   MaxQB; O75795; -.
DR   PaxDb; O75795; -.
DR   PeptideAtlas; O75795; -.
DR   PRIDE; O75795; -.
DR   ProteomicsDB; 50199; -.
DR   DNASU; 7367; -.
DR   Ensembl; ENST00000317746; ENSP00000320401; ENSG00000197888.
DR   GeneID; 7367; -.
DR   KEGG; hsa:7367; -.
DR   UCSC; uc021xov.2; human.
DR   CTD; 7367; -.
DR   DisGeNET; 7367; -.
DR   EuPathDB; HostDB:ENSG00000197888.2; -.
DR   GeneCards; UGT2B17; -.
DR   HGNC; HGNC:12547; UGT2B17.
DR   HPA; HPA045108; -.
DR   MalaCards; UGT2B17; -.
DR   MIM; 601903; gene.
DR   MIM; 612560; phenotype.
DR   neXtProt; NX_O75795; -.
DR   OpenTargets; ENSG00000197888; -.
DR   PharmGKB; PA37189; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   eggNOG; COG1819; LUCA.
DR   GeneTree; ENSGT00940000163930; -.
DR   HOGENOM; HOG000220831; -.
DR   HOVERGEN; HBG004033; -.
DR   InParanoid; O75795; -.
DR   KO; K00699; -.
DR   OMA; NWDQFYS; -.
DR   OrthoDB; 508327at2759; -.
DR   PhylomeDB; O75795; -.
DR   TreeFam; TF315472; -.
DR   BRENDA; 2.4.1.17; 2681.
DR   Reactome; R-HSA-156588; Glucuronidation.
DR   SABIO-RK; O75795; -.
DR   GeneWiki; UGT2B17; -.
DR   GenomeRNAi; 7367; -.
DR   PRO; PR:O75795; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; ENSG00000197888; Expressed in 53 organ(s), highest expression level in sigmoid colon.
DR   Genevisible; O75795; HS.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0052695; P:cellular glucuronidation; IDA:UniProtKB.
DR   GO; GO:0008202; P:steroid metabolic process; TAS:ProtInc.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   Pfam; PF00201; UDPGT; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Endoplasmic reticulum; Glycoprotein;
KW   Glycosyltransferase; Membrane; Microsome; Reference proteome; Signal;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    530       UDP-glucuronosyltransferase 2B17.
FT                                /FTId=PRO_0000036041.
FT   TRANSMEM    495    515       Helical. {ECO:0000255}.
FT   MOD_RES     136    136       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q8BWQ1}.
FT   CARBOHYD     65     65       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    316    316       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    483    483       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   530 AA;  61095 MW;  8E59EBC43CF43760 CRC64;
     MSLKWMSVFL LMQLSCYFSS GSCGKVLVWP TEYSHWINMK TILEELVQRG HEVIVLTSSA
     SILVNASKSS AIKLEVYPTS LTKNDLEDFF MKMFDRWTYS ISKNTFWSYF SQLQELCWEY
     SDYNIKLCED AVLNKKLMRK LQESKFDVLL ADAVNPCGEL LAELLNIPFL YSLRFSVGYT
     VEKNGGGFLF PPSYVPVVMS ELSDQMIFME RIKNMIYMLY FDFWFQAYDL KKWDQFYSEV
     LGRPTTLFET MGKAEMWLIR TYWDFEFPRP FLPNVDFVGG LHCKPAKPLP KEMEEFVQSS
     GENGIVVFSL GSMISNMSEE SANMIASALA QIPQKVLWRF DGKKPNTLGS NTRLYKWLPQ
     NDLLGHPKTK AFITHGGTNG IYEAIYHGIP MVGIPLFADQ HDNIAHMKAK GAALSVDIRT
     MSSRDLLNAL KSVINDPIYK ENIMKLSRIH HDQPVKPLDR AVFWIEFVMR HKGAKHLRVA
     AHNLTWIQYH SLDVIAFLLA CVATMIFMIT KCCLFCFRKL AKTGKKKKRD
//